Bibliographic Details
| Title: |
Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen. |
| Authors: |
de Graaf, Barend H. J., Rudd, Jason J., Wheeler, Michael J., Perry, Ruth M., Bell, Elizabeth M., Osman, Kim, Franklin, F. Christopher H., Franklin-Tong, Vernonica E. |
| Source: |
Nature. 11/23/2006, Vol. 444 Issue 7118, p490-493. 4p. 5 Black and White Photographs, 4 Graphs. |
| Subjects: |
Pollen, Phosphatases, Papaver, Proteins, Calcium ions, Phosphoproteins, Cell death |
| Abstract: |
In higher plants, sexual reproduction involves interactions between pollen and pistil. A key mechanism to prevent inbreeding is self-incompatibility through rejection of incompatible (‘self’) pollen. In Papaver rhoeas, S proteins encoded by the stigma interact with incompatible pollen, triggering a Ca2+-dependent signalling network resulting in pollen tube inhibition and programmed cell death. The cytosolic phosphoprotein p26.1, which has been identified in incompatible pollen, shows rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo. Here we show that p26.1 comprises two proteins, Pr-p26.1a and Pr-p26.1b, which are soluble inorganic pyrophosphatases (sPPases). These proteins have classic Mg2+-dependent sPPase activity, which is inhibited by Ca2+, and unexpectedly can be phosphorylated in vitro. We show that phosphorylation inhibits sPPase activity, establishing a previously unknown mechanism for regulating eukaryotic sPPases. Reduced sPPase activity is predicted to result in the inhibition of many biosynthetic pathways, suggesting that there may be additional mechanisms of self-incompatibility-mediated pollen tube inhibition. We provide evidence that sPPases are required for growth and that self-incompatibility results in an increase in inorganic pyrophosphate, implying a functional role for Pr-p26.1. [ABSTRACT FROM AUTHOR] |
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| Database: |
Psychology and Behavioral Sciences Collection |
